RPC7_YEAST
ID RPC7_YEAST Reviewed; 251 AA.
AC P17890; D6W132; P20838;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC7;
DE Short=RNA polymerase III subunit C7;
DE AltName: Full=DNA-directed RNA polymerase III 31 kDa polypeptide;
DE Short=C31;
GN Name=RPC31; Synonyms=ACP2, RPC8; OrderedLocusNames=YNL151C; ORFNames=N1769;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=S288c / GRF88;
RX PubMed=2201900; DOI=10.1128/mcb.10.9.4737-4743.1990;
RA Mosrin C., Riva M., Beltrame M., Cassar E., Sentenac A., Thuriaux P.;
RT "The RPC31 gene of Saccharomyces cerevisiae encodes a subunit of RNA
RT polymerase C (III) with an acidic tail.";
RL Mol. Cell. Biol. 10:4737-4743(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBY1091 / DKY1;
RX PubMed=2835668; DOI=10.1128/mcb.8.3.1282-1289.1988;
RA Haggren W., Kolodrubetz D.;
RT "The Saccharomyces cerevisiae ACP2 gene encodes an essential HMG1-like
RT protein.";
RL Mol. Cell. Biol. 8:1282-1289(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP REVIEW ON THE RNA POL III COMPLEX.
RX PubMed=10384303; DOI=10.1101/sqb.1998.63.381;
RA Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O.,
RA Werner M., Carles C., Sentenac A.;
RT "The yeast RNA polymerase III transcription machinery: a paradigm for
RT eukaryotic gene activation.";
RL Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Specific peripheric component of RNA polymerase III which synthesizes
CC small RNAs, such as 5S rRNA and tRNAs. C31 is involved in the formation
CC of the initiation complex.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: The acidic domain is essential for its function.
CC -!- SIMILARITY: Belongs to the eukaryotic RPC7 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; X51498; CAA35866.1; -; Genomic_DNA.
DR EMBL; M20315; AAA34390.1; -; Genomic_DNA.
DR EMBL; X92517; CAA63288.1; -; Genomic_DNA.
DR EMBL; Z71427; CAA96038.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10398.1; -; Genomic_DNA.
DR PIR; A36465; RNBY3C.
DR RefSeq; NP_014248.3; NM_001182989.3.
DR PDB; 5FJ8; EM; 3.90 A; Q=1-69.
DR PDB; 5FJ9; EM; 4.60 A; Q=1-69.
DR PDB; 5FJA; EM; 4.65 A; Q=1-69.
DR PDB; 6CNB; EM; 4.10 A; Q=1-251.
DR PDB; 6CNC; EM; 4.10 A; Q=1-251.
DR PDB; 6CND; EM; 4.80 A; Q=1-251.
DR PDB; 6CNF; EM; 4.50 A; Q=1-251.
DR PDB; 6EU0; EM; 4.00 A; Q=1-251.
DR PDB; 6EU1; EM; 3.40 A; Q=1-251.
DR PDB; 6EU2; EM; 3.40 A; Q=1-251.
DR PDB; 6EU3; EM; 3.30 A; Q=1-251.
DR PDB; 6F40; EM; 3.70 A; Q=1-251.
DR PDB; 6F41; EM; 4.30 A; Q=1-251.
DR PDB; 6F42; EM; 5.50 A; Q=1-251.
DR PDB; 6F44; EM; 4.20 A; Q=1-251.
DR PDB; 6TUT; EM; 3.25 A; Q=1-251.
DR PDBsum; 5FJ8; -.
DR PDBsum; 5FJ9; -.
DR PDBsum; 5FJA; -.
DR PDBsum; 6CNB; -.
DR PDBsum; 6CNC; -.
DR PDBsum; 6CND; -.
DR PDBsum; 6CNF; -.
DR PDBsum; 6EU0; -.
DR PDBsum; 6EU1; -.
DR PDBsum; 6EU2; -.
DR PDBsum; 6EU3; -.
DR PDBsum; 6F40; -.
DR PDBsum; 6F41; -.
DR PDBsum; 6F42; -.
DR PDBsum; 6F44; -.
DR PDBsum; 6TUT; -.
DR AlphaFoldDB; P17890; -.
DR SMR; P17890; -.
DR BioGRID; 35678; 181.
DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR DIP; DIP-6687N; -.
DR IntAct; P17890; 8.
DR MINT; P17890; -.
DR STRING; 4932.YNL151C; -.
DR iPTMnet; P17890; -.
DR MaxQB; P17890; -.
DR PaxDb; P17890; -.
DR PRIDE; P17890; -.
DR EnsemblFungi; YNL151C_mRNA; YNL151C; YNL151C.
DR GeneID; 855571; -.
DR KEGG; sce:YNL151C; -.
DR SGD; S000005095; RPC31.
DR VEuPathDB; FungiDB:YNL151C; -.
DR eggNOG; ENOG502RZ0V; Eukaryota.
DR HOGENOM; CLU_072641_2_0_1; -.
DR InParanoid; P17890; -.
DR OMA; FDPFHGM; -.
DR BioCyc; YEAST:G3O-33168-MON; -.
DR Reactome; R-SCE-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-SCE-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR PRO; PR:P17890; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P17890; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; IDA:ComplexPortal.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IDA:ComplexPortal.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:SGD.
DR InterPro; IPR024661; RNA_pol_III_Rpc31.
DR PANTHER; PTHR15367; PTHR15367; 1.
DR Pfam; PF11705; RNA_pol_3_Rpc31; 1.
DR PIRSF; PIRSF000777; RNA_polIII_C31; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription; Transferase.
FT CHAIN 1..251
FT /note="DNA-directed RNA polymerase III subunit RPC7"
FT /id="PRO_0000073980"
FT REGION 186..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 12
FT /note="G -> R (in Ref. 2; AAA34390)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="D -> H (in Ref. 2; AAA34390)"
FT /evidence="ECO:0000305"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6EU1"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:6EU1"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 105..109
FT /evidence="ECO:0007829|PDB:6TUT"
SQ SEQUENCE 251 AA; 27724 MW; 33A7D8EAE47793E1 CRC64;
MSSYRGGSRG GGSNYMSNLP FGLGYGDVGK NHITEFPSIP LPINGPITNK ERSLAVKYIN
FGKTVKDGPF YTGSMSLIID QQENSKSGKR KPNIILDEDD TNDGIERYSD KYLKKRKIGI
SIDDHPYNLN LFPNELYNVM GINKKKLLAI SKFNNADDVF TGTGLQDENI GLSMLAKLKE
LAEDVDDAST GDGAAKGSKT GEGEDDDLAD DDFEEDEDEE DDDDYNAEKY FNNGDDDDYG
DEEDPNEEAA F
